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P26883

- FKB1A_MOUSE

UniProt

P26883 - FKB1A_MOUSE

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

Fkbp1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by both FK506 and rapamycin.

GO - Molecular functioni

  1. calcium channel inhibitor activity Source: RefGenome
  2. drug binding Source: MGI
  3. FK506 binding Source: MGI
  4. ion channel binding Source: BHF-UCL
  5. peptidyl-prolyl cis-trans isomerase activity Source: RefGenome
  6. protein homodimerization activity Source: MGI

GO - Biological processi

  1. chaperone-mediated protein folding Source: RefGenome
  2. cytokine-mediated signaling pathway Source: MGI
  3. heart morphogenesis Source: BHF-UCL
  4. heart trabecula formation Source: BHF-UCL
  5. muscle contraction Source: MGI
  6. negative regulation of protein phosphorylation Source: MGI
  7. negative regulation of release of sequestered calcium ion into cytosol Source: RefGenome
  8. protein peptidyl-prolyl isomerization Source: RefGenome
  9. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  10. release of sequestered calcium ion into cytosol Source: MGI
  11. response to caffeine Source: MGI
  12. response to iron ion Source: Ensembl
  13. T cell proliferation Source: MGI
  14. ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiREACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_224217. TGFBR1 LBD Mutants in Cancer.
REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_224802. TGFBR1 KD Mutants in Cancer.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
Short name:
PPIase FKBP1A
Alternative name(s):
12 kDa FK506-binding protein
Short name:
12 kDa FKBP
Short name:
FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name:
FKBP-1A
Immunophilin FKBP12
Rotamase
Gene namesi
Name:Fkbp1a
Synonyms:Fkbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:95541. Fkbp1a.

Subcellular locationi

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. membrane Source: MGI
  3. sarcoplasmic reticulum membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1APRO_0000075290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei53 – 531N6-acetyllysine; alternate1 Publication
Modified residuei53 – 531N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26883.
PaxDbiP26883.
PRIDEiP26883.

PTM databases

PhosphoSiteiP26883.

Expressioni

Gene expression databases

BgeeiP26883.
CleanExiMM_FKBP1A.
ExpressionAtlasiP26883. baseline and differential.
GenevestigatoriP26883.

Interactioni

Subunit structurei

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation (By similarity). Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3 (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1).By similarity1 Publication

Protein-protein interaction databases

BioGridi199682. 3 interactions.
DIPiDIP-29707N.
IntActiP26883. 3 interactions.
MINTiMINT-4095099.

Structurei

3D structure databases

ProteinModelPortaliP26883.
SMRiP26883. Positions 2-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10889PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiP26883.
KOiK09568.
OMAiSPQKGDT.
OrthoDBiEOG7ZGX5T.
TreeFamiTF105291.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26883-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT
60 70 80 90 100
LGKQEVIRGW EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF

DVELLKLE
Length:108
Mass (Da):11,923
Last modified:January 23, 2007 - v2
Checksum:i8C265ED5803F6987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60203 mRNA. Translation: CAA42762.1.
U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1.
AF483488 mRNA. Translation: AAL90762.1.
AF483489 mRNA. Translation: AAL90763.1.
AK002777 mRNA. Translation: BAB22351.1.
AK010693 mRNA. Translation: BAB27125.1.
AK019362 mRNA. Translation: BAB31680.1.
AK154751 mRNA. Translation: BAE32804.1.
AK168333 mRNA. Translation: BAE40271.1.
AK169186 mRNA. Translation: BAE40963.1.
AK169242 mRNA. Translation: BAE41008.1.
BC004671 mRNA. Translation: AAH04671.1.
CCDSiCCDS16869.1.
PIRiJH0528.
RefSeqiNP_032045.1. NM_008019.3.
UniGeneiMm.278458.
Mm.487732.

Genome annotation databases

EnsembliENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
GeneIDi14225.
KEGGimmu:14225.
UCSCiuc008ndy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60203 mRNA. Translation: CAA42762.1 .
U65100 , U65098 , U65099 Genomic DNA. Translation: AAB17554.1 .
AF483488 mRNA. Translation: AAL90762.1 .
AF483489 mRNA. Translation: AAL90763.1 .
AK002777 mRNA. Translation: BAB22351.1 .
AK010693 mRNA. Translation: BAB27125.1 .
AK019362 mRNA. Translation: BAB31680.1 .
AK154751 mRNA. Translation: BAE32804.1 .
AK168333 mRNA. Translation: BAE40271.1 .
AK169186 mRNA. Translation: BAE40963.1 .
AK169242 mRNA. Translation: BAE41008.1 .
BC004671 mRNA. Translation: AAH04671.1 .
CCDSi CCDS16869.1.
PIRi JH0528.
RefSeqi NP_032045.1. NM_008019.3.
UniGenei Mm.278458.
Mm.487732.

3D structure databases

ProteinModelPortali P26883.
SMRi P26883. Positions 2-108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199682. 3 interactions.
DIPi DIP-29707N.
IntActi P26883. 3 interactions.
MINTi MINT-4095099.

PTM databases

PhosphoSitei P26883.

Proteomic databases

MaxQBi P26883.
PaxDbi P26883.
PRIDEi P26883.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044011 ; ENSMUSP00000037206 ; ENSMUSG00000032966 .
GeneIDi 14225.
KEGGi mmu:14225.
UCSCi uc008ndy.1. mouse.

Organism-specific databases

CTDi 2280.
MGIi MGI:95541. Fkbp1a.

Phylogenomic databases

eggNOGi COG0545.
GeneTreei ENSGT00760000119159.
HOGENOMi HOG000154887.
HOVERGENi HBG051623.
InParanoidi P26883.
KOi K09568.
OMAi SPQKGDT.
OrthoDBi EOG7ZGX5T.
TreeFami TF105291.

Enzyme and pathway databases

Reactomei REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_203510. TGF-beta receptor signaling activates SMADs.
REACT_224217. TGFBR1 LBD Mutants in Cancer.
REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_224802. TGFBR1 KD Mutants in Cancer.

Miscellaneous databases

NextBioi 285479.
PROi P26883.
SOURCEi Search...

Gene expression databases

Bgeei P26883.
CleanExi MM_FKBP1A.
ExpressionAtlasi P26883. baseline and differential.
Genevestigatori P26883.

Family and domain databases

InterProi IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view ]
PANTHERi PTHR10516. PTHR10516. 1 hit.
Pfami PF00254. FKBP_C. 1 hit.
[Graphical view ]
PROSITEi PS50059. FKBP_PPIASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced amino acid sequence."
    Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.
    Gene 109:255-258(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  2. Shou W., Bao S., Mathews L.S., Matzuk M.M.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 129/Sv.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ILS and ISS.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Hippocampus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
    Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
    Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFKB1A_MOUSE
AccessioniPrimary (citable) accession number: P26883
Secondary accession number(s): Q545E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3